UniProtKB/Swiss-Prot P21462: Variant p.Val101Leu

N-formyl peptide receptor 1
Gene: FPR1
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Variant information Variant position:

101 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B The variants are classified into three categories: LP/P, LB/B and US.

LP/P: likely pathogenic or pathogenic.
LB/B: likely benign or benign.
US: uncertain significance

Residue change:

From Valine (V) to Leucine (L) at position 101 (V101L, p.Val101Leu). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties:

Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:

Lowest score: -4 (low probability of substitution).
Highest score: 11 (high probability of substitution).

More information can be found on the following page
Polymorphism:

Common FPR1 variations may have been selected to enhance human resistance to infections. FRP1 p.Arg190Trp is identified as an allele that protect neutrophils from destruction by Y. pestis type III secretion system. Additional information on the polymorphism described.
Other resources:

Links to websites of interest for the variant.

Variant rs2070745 [ dbSNP | Ensembl ]

Sequence information Variant position:

101 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

350 The length of the canonical sequence.
Location on the sequence:

FMVRKAMGGHWPFGWFLCKF V FTIVDINLFGSVFLIALIAL The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation:

The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         FMVRKAMGGHWPFGWFLCKFVFTIVDINLFGSVFLIALIAL

Mouse                         YIASMVMGGHWPFGWFMCKFIYTVIDINLFGSVFLIALIAL

Rabbit                        FIVTKALGGHWPFGWFLCKFVFTIVDINLFGSVFLIALIAL

Sequence annotation in neighborhood:

The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:

Type: the type of sequence feature.
Positions: endpoints of the sequence feature.
Description: contains additional information about the feature.

Type	Positions	Description
Chain	1 – 350	N-formyl peptide receptor 1
Transmembrane	101 – 121	Helical; Name=3
Binding site	106 – 106
Binding site	106 – 106
Disulfide bond	98 – 176
Mutagenesis	81 – 81	F -> A. Slightly decreases intracellular cAMP reduction upon stimulation with N-formylated fMLF peptide.
Mutagenesis	84 – 84	R -> D. Decreases intracellular cAMP reduction upon stimulation with N-formyl peptide fMLFII.
Mutagenesis	102 – 102	F -> A. Slightly decreases intracellular cAMP reduction upon stimulation with N-formyl peptide fMLF. Slightly decreases the agonist potency of non-formylated WKYMVm peptide.
Mutagenesis	102 – 102	F -> H. Decreases intracellular cAMP reduction upon stimulation with N-formyl peptide fMLFII.
Mutagenesis	106 – 106	D -> A. Abolishes the response to N-formyl peptides fMLF, fMIFL and fMLFII.
Mutagenesis	106 – 106	D -> N. Abolishes the response to N-formyl peptides fMLF and fMIFL.
Mutagenesis	109 – 109	L -> A. Slightly decreases intracellular cAMP reduction upon stimulation with N-formyl peptide fMLF. Decreases the agonist potency of non-formylated WKYMVm peptide.
Mutagenesis	110 – 110	F -> A. Slightly decreases intracellular cAMP reduction upon stimulation with N-formyl peptide fMLF.
Helix	95 – 128

Literature citations
Synthesis and use of a novel N-formyl peptide derivative to isolate a human N-formyl peptide receptor cDNA.
Boulay F.; Tardif M.; Brouchon L.; Vignais P.;
Biochem. Biophys. Res. Commun. 168:1103-1109(1990)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; FUNCTION; VARIANTS LEU-101 AND ALA-346;
The human N-formylpeptide receptor. Characterization of two cDNA isolates and evidence for a new subfamily of G-protein-coupled receptors.
Boulay F.; Tardif M.; Brouchon L.; Vignais P.;
Biochemistry 29:11123-11133(1990)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; FUNCTION; SUBCELLULAR LOCATION; VARIANTS LEU-101 AND ALA-346;

Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.